S
Stephen J. Tucker
Researcher at University of Oxford
Publications - 158
Citations - 9006
Stephen J. Tucker is an academic researcher from University of Oxford. The author has contributed to research in topics: Gating & Potassium channel. The author has an hindex of 47, co-authored 143 publications receiving 8165 citations. Previous affiliations of Stephen J. Tucker include Kyoto University & Pontifical Catholic University of Chile.
Papers
More filters
Journal ArticleDOI
Altered functional properties of a missense variant in the TRESK K+ channel (KCNK18) associated with migraine and intellectual disability.
Paola Imbrici,Ehsan Nematian-Ardestani,Sonia Hasan,Mauro Pessia,Mauro Pessia,Stephen J. Tucker,Maria Cristina D'Adamo +6 more
TL;DR: The results show although these mutant channels retain their K+ selectivity and calcineurin-dependent regulation, the variant causes an overall dramatic loss of TRESK channel function as well as an initial dominant-negative effect when co-expressed with wild-type channels in Xenopus laevis oocytes.
Journal ArticleDOI
Water Nanoconfined in a Hydrophobic Pore: Molecular Dynamics Simulations of Transmembrane Protein 175 and the Influence of Water Models.
TL;DR: Water molecules within biological ion channels are in a nanoconfined environment and therefore exhibit behaviors which differ from that of bulk water as discussed by the authors, and the phenomenon of hydrophoresis is investigated.
Journal ArticleDOI
Peptide backbone mutagenesis of putative gating hinges in a potassium ion channel.
TL;DR: This study addressed the relative contribution of putative glycine gating hinges in inwardly rectifying potassium channels by using unnatural amino acid mutagenesis to introduce a-hydroxyacetic acid (aG) and thereby an amideto-ester mutation into the backbone of Kir2.
Journal ArticleDOI
State-dependent network connectivity determines gating in a K+ channel.
Murali K. Bollepalli,Philip W. Fowler,Markus Rapedius,Lijun Shang,Mark S.P. Sansom,Stephen J. Tucker,Thomas Baukrowitz +6 more
TL;DR: This mutagenic perturbation analysis uncovered an extensive, state-dependent network of physically interacting residues that stabilizes the pre-open and open states of the channel, but fragments upon channel closure.
Posted ContentDOI
A unique lower X-gate in TASK channels traps inhibitors within the vestibule
Karin E. J. Rödström,Aytug K. Kiper,Wei Zhang,Wei Zhang,Susanne Rinné,Ashley C. W. Pike,Matthias Goldstein,Linus J. Conrad,Martina Delbeck,Michael G. Hahn,Heinrich Meier,Magdalena Platzk,A. Quigley,David Speedman,Leela Shrestha,Shubhashish M.M. Mukhopadhyay,N.A. Burgess-Brown,Stephen J. Tucker,Thomas Mueller,Niels Decher,Elisabeth P. Carpenter +20 more
TL;DR: The structure of TASK-1 is presented, revealing a unique lower gate created by interaction of the two crossed C-terminal M4 transmembrane helices at the vestibule entrance, which is designated as an ‟X-gate”, which explains many aspects of their unusual physiological and pharmacological behaviour.